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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Toxic Reactions: Overview01:26

Toxic Reactions: Overview

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When toxic substances penetrate the human body, they disseminate to various tissues, undergoing metabolic changes. This process yields reactive metabolites that may covalently bind with specific target molecules, resulting in toxicity.
Toxicity falls into two primary categories: local and systemic.
Local toxicity appears at the exposure site, such as protein denaturation caused by caustic substances.
In contrast, systemic toxicity requires the toxic agent's absorption and distribution,...
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Toxicity Testing in Animals01:23

Toxicity Testing in Animals

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Toxicity tests in animals are grounded on two main assumptions: first, the effects observed in laboratory animals can be extrapolated to humans, especially when adjusted for body surface area; second, high-dose exposure in animals is essential to identify potential human hazards from lower doses. This is based on the quantal dose-response concept, which faces the challenge of extrapolating results from relatively few test animals to much larger human populations. For example, a 0.01% incidence...
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Physical Properties of Amines01:26

Physical Properties of Amines

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Amines with low molecular weight are usually gaseous at room temperature, while those with high molecular weight are liquid or solids in nature. Usually, low molecular weight amines have a rotten fish-like smell. Diamines typically have a pungent smell. For instance, cadaverine and putrescine, depicted in Figure 1, are two molecules responsible for decaying tissue.
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Lysosomal Hydrolases01:22

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Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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Why are Functional Amyloids Non-Toxic in Humans?

Matthew P Jackson1, Eric W Hewitt2

  • 1School of Molecular and Cellular Biology and Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK. m.p.jackson@leeds.ac.uk.

Biomolecules
|September 23, 2017
PubMed
Summary
This summary is machine-generated.

Cells can produce functional amyloids, which are protein aggregates, without harm. Understanding how cells manage amyloid formation offers insights into preventing toxic amyloid diseases.

Keywords:
amyloidsfibrilfunctional amyloidoligomerstoxicity

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Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Amyloid fibrils were initially linked to human diseases called amyloidoses, characterized by protein misfolding.
  • Recent research has revealed that amyloid fibrils also serve essential physiological functions in humans.

Purpose of the Study:

  • To explore the remarkable ability of cells to produce functional amyloids without toxicity.
  • To investigate the mechanisms cells employ to prevent or mitigate amyloid-associated toxicity.

Main Methods:

  • Review of existing literature on amyloid formation, functional amyloids, and cellular defense mechanisms.
  • Analysis of proposed strategies for controlling amyloidogenic processes within cells.

Main Results:

  • Cells possess multiple strategies to prevent amyloid toxicity during functional amyloid production.
  • These strategies include regulating protein levels, minimizing toxic oligomers, compartmentalizing amyloids, and controlling fibril assembly/disassembly.

Conclusions:

  • The mechanisms protecting against functional amyloid toxicity are diverse and sophisticated.
  • Understanding these protective mechanisms could pave the way for novel therapeutic strategies against amyloid-related diseases.